|
Name |
Accession |
Description |
Interval |
E-value |
| PA_CoA_ligase |
TIGR02155 |
phenylacetate-CoA ligase; Phenylacetate-CoA ligase (PA-CoA ligase) catalyzes the first step in ... |
11-432 |
0e+00 |
|
phenylacetate-CoA ligase; Phenylacetate-CoA ligase (PA-CoA ligase) catalyzes the first step in aromatic catabolism of phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Often located in a conserved gene cluster with enzymes involved in phenylacetic acid activation (paaG/H/I/J), phenylacetate-CoA ligase has been found among the proteobacteria as well as in gram positive prokaryotes. In the B-subclass proteobacterium Azoarcus evansii, phenylacetate-CoA ligase has been shown to be induced under aerobic and anaerobic growth conditions. It remains unclear however, whether this induction is due to the same enzyme or to another isoenzyme restricted to specific anaerobic growth conditions. [Energy metabolism, Other]
Pssm-ID: 131210 [Multi-domain] Cd Length: 422 Bit Score: 826.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 11 ETASIDELQALQTARLKWTLHHAYNNVPMYKRKFDAAGVHPDDFTELADLQKFPCTTKQDLRDNYPFDTFAVPMEQVVRI 90
Cdd:TIGR02155 1 ETASLDELRALQTQRLKWTVKHAYENVPHYRKAFDAAGVHPDDLQSLSDLAKFPFTQKHDLRDNYPFGLFAVPREQVVRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 91 HASSGTTGKPTVVGYTQNDIDNWANIVARSLRAAGGSAKDKIHVAYGYGLFTGGLGAHYGAERLGATVIPMSGGQTEKQA 170
Cdd:TIGR02155 81 HASSGTTGKPTVVGYTQNDIDTWSSVVARSIRAAGGRPGDLIHNAYGYGLFTGGLGAHYGAEKLGCTVVPISGGQTEKQV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 171 QLIRDFQPDMIMVTPSYCLNLIEELERqMGGDASACSLRVGVFGAEPWTQAMRREIEKRLGITALDIYGLSEVMGPGVAM 250
Cdd:TIGR02155 161 QLIQDFKPDIIMVTPSYMLNLLEELKR-MGIDPAQTSLQVGIFGAEPWTNAMRKEIEARLGMKATDIYGLSEVIGPGVAM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 251 ECLETADGPTIWEDHFYPEIVNPNDGTPLADGEQGELLFTTLTKEALPVIRYRTRDLTRLLPGTARTMRRMDRISGRSDD 330
Cdd:TIGR02155 240 ECVETQDGLHIWEDHFYPEIIDPHTGEVLPDGEEGELVFTTLTKEALPVIRYRTRDLTRLLPGTARTMRRMDRITGRSDD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 331 MLIIRGVNVFPSQLEEEIVKFEHLSPHYQLEVNRRGHLDSLSVKVELK-QSSLTLTHEQRCQVCHQLRHRIKSMVGISTD 409
Cdd:TIGR02155 320 MLIIRGVNVFPTQLEEVILKMDELSPHYQLELTRNGHMDELTLKVELKpESYTLRLHEQASLLAGEIQHTIKQEVGVSMD 399
|
410 420
....*....|....*....|...
gi 515953928 410 VMIVNCGSIPRSEGKACRVFDLR 432
Cdd:TIGR02155 400 VHLVEPGSLPRSEGKARRVVDLR 422
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
8-433 |
0e+00 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 704.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 8 DPIETASIDELQALQTARLKWTLHHAYNNVPMYKRKFDAAGVHPDDFTELADLQKFPCTTKQDLRDNYPFDTFAVPMEQV 87
Cdd:cd05913 1 EEIETMSRDELDALQLARLKWTVRHAYENVPFYRRKFAAAGIDPDDIKSLDDLRKLPFTTKEDLRDNYPFGLFAVPREKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 88 VRIHASSGTTGKPTVVGYTQNDIDNWANIVARSLRAAGGSAKDKIHVAYGYGLFTGGLGAHYGAERLGATVIPMSGGQTE 167
Cdd:cd05913 81 VRIHASSGTTGKPTVVGYTKNDLDVWAELVARCLDAAGVTPGDRVQNAYGYGLFTGGLGFHYGAERLGALVIPAGGGNTE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 168 KQAQLIRDFQPDMIMVTPSYCLNLIEELERQmGGDASACSLRVGVFGAEPWTQAMRREIEKRLGITALDIYGLSEVMGPG 247
Cdd:cd05913 161 RQLQLIKDFGPTVLCCTPSYALYLAEEAEEE-GIDPRELSLKVGIFGAEPWTEEMRKRIERRLGIKAYDIYGLTEIIGPG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 248 VAMECLEtADGPTIWEDHFYPEIVNPNDGTPLADGEQGELLFTTLTKEALPVIRYRTRDLTRLLPGTA---RTMRRMDRI 324
Cdd:cd05913 240 VAFECEE-KDGLHIWEDHFIPEIIDPETGEPVPPGEVGELVFTTLTKEAMPLIRYRTRDITRLLPGPCpcgRTHRRIDRI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 325 SGRSDDMLIIRGVNVFPSQLEEEIVKFEHLSPHYQLEVNRRGHLDSLSVKVELKQSSltLTHEQRCQVCHQLRHRIKSMV 404
Cdd:cd05913 319 TGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGPHYQLILTRQEHLDELTIKVEVRPEA--DDDEKLEALKQRLERHIKSVL 396
|
410 420
....*....|....*....|....*....
gi 515953928 405 GISTDVMIVNCGSIPRSEGKACRVFDLRK 433
Cdd:cd05913 397 GVTVEVELVEPGSLPRSEGKAKRVIDKRK 425
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
8-431 |
0e+00 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 677.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 8 DPIETASIDELQALQTARLKWTLHHAYNNVPMYKRKFDAAGVHPDDFTELADLQKFPCTTKQDLRDNYPFDTFAVPMEQV 87
Cdd:COG1541 6 NPIETLSREELEALQLERLRATVARAYENSPFYRRKFDEAGVDPDDIKSLEDLAKLPFTTKEDLRDNYPFGLFAVPLEEI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 88 VRIHASSGTTGKPTVVGYTQNDIDNWANIVARSLRAAGGSAKDKIHVAYGYGLFTGGLGAHYGAERLGATVIPMSGGQTE 167
Cdd:COG1541 86 VRIHASSGTTGKPTVVGYTRKDLDRWAELFARSLRAAGVRPGDRVQNAFGYGLFTGGLGLHYGAERLGATVIPAGGGNTE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 168 KQAQLIRDFQPDMIMVTPSYCLNLIEELERqMGGDASACSLRVGVFGAEPWTQAMRREIEKRLGITALDIYGLSEvMGPG 247
Cdd:COG1541 166 RQLRLMQDFGPTVLVGTPSYLLYLAEVAEE-EGIDPRDLSLKKGIFGGEPWSEEMRKEIEERWGIKAYDIYGLTE-VGPG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 248 VAMEClETADGPTIWEDHFYPEIVNPNDGTPLADGEQGELLFTTLTKEALPVIRYRTRDLTRLLPG---TARTMRRMDRI 324
Cdd:COG1541 244 VAYEC-EAQDGLHIWEDHFLVEIIDPETGEPVPEGEEGELVVTTLTKEAMPLIRYRTGDLTRLLPEpcpCGRTHPRIGRI 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 325 SGRSDDMLIIRGVNVFPSQLEEEIVKFEHLSPHYQLEVNRRGHLDSLSVKVELKQSsltlthEQRCQVCHQLRHRIKSMV 404
Cdd:COG1541 323 LGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVELAPG------ASLEALAEAIAAALKAVL 396
|
410 420
....*....|....*....|....*..
gi 515953928 405 GISTDVMIVNCGSIPRSEGKACRVFDL 431
Cdd:COG1541 397 GLRAEVELVEPGSLPRSEGKAKRVIDR 423
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
86-350 |
3.82e-39 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 143.58 E-value: 3.82e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 86 QVVRIHASSGTTGKPTVVGYTQNDIDNWANIVARSLraaGGSAKDKIHVAYGYGlFTGGLGAHYGAERLGATVIPMSGGQ 165
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASG---GLTEGDVFLSTLPLF-HIGGLFGLLGALLAGGTVVLLPKFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 166 TEKQAQLIRDFQPDMIMVTPSYCLNLIEELERQmGGDASacSLRVGVFGAEPWTQAMRREIEKRLGITALDIYGLSEVMG 245
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTLLARLLKAPESA-GYDLS--SLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 246 PGVAM------ECLETADGPTiweDHFYPEIVNPnDGTPLADGEQGELLFTT------------LTKEALPVIRYRTRDL 307
Cdd:cd04433 154 TVATGppdddaRKPGSVGRPV---PGVEVRIVDP-DGGELPPGEIGELVVRGpsvmkgywnnpeATAAVDEDGWYRTGDL 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 515953928 308 TRLLPgtartmrrmD---RISGRSDDMLIIRGVNVFPSQLEEEIVK 350
Cdd:cd04433 230 GRLDE---------DgylYIVGRLKDMIKSGGENVYPAEVEAVLLG 266
|
|
| AMP-binding_C_2 |
pfam14535 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
336-432 |
1.79e-37 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 434024 [Multi-domain] Cd Length: 96 Bit Score: 131.83 E-value: 1.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 336 GVNVFPSQLEEEIVKFEHLSPHYQLEVNRRGHLDSLSVKVELKQsSLTLTHEQRCQVCHQLRHRIKSMVGISTDVMIVNC 415
Cdd:pfam14535 1 GVNVFPSQIEEVLLEIPGVGPEYQIIVTREGGLDELEVKVEVAE-GFSDEIKDLEALEKRIAKELKSVLGVSVKVELVEP 79
|
90
....*....|....*..
gi 515953928 416 GSIPRSEGKACRVFDLR 432
Cdd:pfam14535 80 GTLPRSEGKAKRVIDLR 96
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
93-348 |
2.83e-26 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 110.29 E-value: 2.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 93 SSGTTGKPTVVGYTQNdidNWANIVARSLRAAGGSAKDKIHVA----YGYGLFTGGLGAHYgaerLGATVIPMSGGQTEK 168
Cdd:COG0318 108 TSGTTGRPKGVMLTHR---NLLANAAAIAAALGLTPGDVVLVAlplfHVFGLTVGLLAPLL----AGATLVLLPRFDPER 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 169 QAQLIRDFQPDMIMVTPSYCLNLIEELERQmGGDASacSLRVGVFGAEPWTQAMRREIEKRLGITALDIYGLSEvMGPGV 248
Cdd:COG0318 181 VLELIERERVTVLFGVPTMLARLLRHPEFA-RYDLS--SLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTE-TSPVV 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 249 AMECLETADGPTIWEDHFYP----EIVNPnDGTPLADGEQGELLF------------TTLTKEALPVIRYRTRDLtrllp 312
Cdd:COG0318 257 TVNPEDPGERRPGSVGRPLPgvevRIVDE-DGRELPPGEVGEIVVrgpnvmkgywndPEATAEAFRDGWLRTGDL----- 330
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 515953928 313 GtartmrRMD-----RISGRSDDMLIIRGVNVFPSQLEEEI 348
Cdd:COG0318 331 G------RLDedgylYIVGRKKDMIISGGENVYPAEVEEVL 365
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
93-335 |
6.27e-17 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 82.36 E-value: 6.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 93 SSGTTGKPT-VVGYTQNDIDNWANIVARSLRAAGGSAKDKIH----VAYGYGLFTGGLGAHYgaerLGATVIPMSGGQT- 166
Cdd:pfam00501 163 TSGTTGKPKgVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLstlpLFHDFGLSLGLLGPLL----AGATVVLPPGFPAl 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 167 --EKQAQLIRDFQPDMIMVTPSYcLNLIEELERQMGGDASacSLRVGVFGAEPWTQAMRREIEKRLGITALDIYGLSEvM 244
Cdd:pfam00501 239 dpAALLELIERYKVTVLYGVPTL-LNMLLEAGAPKRALLS--SLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTE-T 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 245 GPGVAMECLETAD-------GPTIWEDHFYpeIVNPNDGTPLADGEQGELLF------------TTLTKEALPVIR-YRT 304
Cdd:pfam00501 315 TGVVTTPLPLDEDlrslgsvGRPLPGTEVK--IVDDETGEPVPPGEPGELCVrgpgvmkgylndPELTAEAFDEDGwYRT 392
|
250 260 270
....*....|....*....|....*....|....
gi 515953928 305 RDLTRLLPgtartmrrmD---RISGRSDDMLIIR 335
Cdd:pfam00501 393 GDLGRRDE---------DgylEIVGRKKDQIKLG 417
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
81-352 |
9.57e-13 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 69.56 E-value: 9.57e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 81 AVPMEQVVRIHASSGTTGKPTVVGYTQndiDNWANIVARSLRAAGGSAKDK-IHVAygyGLF-TGGLGAHYGAERL-GAT 157
Cdd:cd17631 94 KVLFDDLALLMYTSGTTGRPKGAMLTH---RNLLWNAVNALAALDLGPDDVlLVVA---PLFhIGGLGVFTLPTLLrGGT 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 158 VIPMSGGQTEKQAQLIRDFQPDMIMVTPSYcLNLIEELERQMGGDASacSLRVGVFGAEPWTQAMRREIEKRlGITALDI 237
Cdd:cd17631 168 VVILRKFDPETVLDLIERHRVTSFFLVPTM-IQALLQHPRFATTDLS--SLRAVIYGGAPMPERLLRALQAR-GVKFVQG 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 238 YGLSEvMGPGVAMecLETadgptiwEDHF-------YP------EIVNPnDGTPLADGEQGELlfttltkealpVIRYRT 304
Cdd:cd17631 244 YGMTE-TSPGVTF--LSP-------EDHRrklgsagRPvffvevRIVDP-DGREVPPGEVGEI-----------VVRGPH 301
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 305 rdltrLLPG-------TARTMR----------RMDR-----ISGRSDDMLIIRGVNVFPSQLEEEIVKFE 352
Cdd:cd17631 302 -----VMAGywnrpeaTAAAFRdgwfhtgdlgRLDEdgylyIVDRKKDMIISGGENVYPAEVEDVLYEHP 366
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
85-350 |
8.09e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 66.15 E-value: 8.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 85 EQVVRIHASSGTTGKPTVVGYTQNDIDNWANIVARSLraaGGSAKDKIHVAYG----YGLFTGGLGA-HYGAerlgATVI 159
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNNGYFIGERL---GLTEQDRLCIPVPlfhcFGSVLGVLAClTHGA----TMVF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 160 PMSGGQTEKQAQLIRDFQPDMIMVTPSYclnLIEELERQMGGDASACSLRVGVFGAEPWTQAMRREIEKRLGITALDI-Y 238
Cdd:cd05917 75 PSPSFDPLAVLEAIEKEKCTALHGVPTM---FIAELEHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIaY 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 239 GLSEVmGPGVAMEclETADGP-----TIWE--DHFYPEIVNPNDGTPLADGEQGELL---FTTL---------TKEALPV 299
Cdd:cd05917 152 GMTET-SPVSTQT--RTDDSIekrvnTVGRimPHTEAKIVDPEGGIVPPVGVPGELCirgYSVMkgywndpekTAEAIDG 228
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 515953928 300 IR-YRTRDLtrllpGTartmrrMD-----RISGRSDDMLIIRGVNVFPSQLEEEIVK 350
Cdd:cd05917 229 DGwLHTGDL-----AV------MDedgycRIVGRIKDMIIRGGENIYPREIEEFLHT 274
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
93-357 |
8.02e-11 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 63.55 E-value: 8.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 93 SSGTTGKPTVVGYTQNDIdnWANIVARSLRAAGGSaKDKIHVAYGYGLFTGGLGAHYGAERLGATVIPMSGGQTEKQAQL 172
Cdd:cd05903 101 TSGTTGEPKGVMHSHNTL--SASIRQYAERLGLGP-GDVFLVASPMAHQTGFVYGFTLPLLLGAPVVLQDIWDPDKALAL 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 173 IRDFQPDMIMVTPSYCLNLIEELERQmggDASACSLRVGVFGAEPWTQAMRREIEKRLGITALDIYGLSEVMGpgvAMEC 252
Cdd:cd05903 178 MREHGVTFMMGATPFLTDLLNAVEEA---GEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPG---AVTS 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 253 LETADGPTIWEDHFYP----EI-VNPNDGTPLADGEQGELLFTT------------LTKEALPVIRYRTRDLTrllpgta 315
Cdd:cd05903 252 ITPAPEDRRLYTDGRPlpgvEIkVVDDTGATLAPGVEGELLSRGpsvflgyldrpdLTADAAPEGWFRTGDLA------- 324
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 515953928 316 rtmrRMD-----RISGRSDDmLIIRGVNVFPSqLEEEIVKFEHLSPH 357
Cdd:cd05903 325 ----RLDedgylRITGRSKD-IIIRGGENIPV-LEVEDLLLGHPGVI 365
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
94-353 |
4.44e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 58.38 E-value: 4.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 94 SGTTGKPTVVGYT-QNDIDN---WANIvarslraAGGSAKDKI-------HVaYGYglfTGGLGAHYGAerlGATVIPMS 162
Cdd:PRK07656 175 SGTTGRPKGAMLThRQLLSNaadWAEY-------LGLTEGDRYlaanpffHV-FGY---KAGVNAPLMR---GATILPLP 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 163 GGQTEKQAQLIRDFQPDMIMVTPSYCLNLieeLERQMGGDASACSLRVGVFGAEPWTQAMRREIEKRLGI-TALDIYGLS 241
Cdd:PRK07656 241 VFDPDEVFRLIETERITVLPGPPTMYNSL---LQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVdIVLTGYGLS 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 242 EVMG------PGVAMECLETADGPTIWedHFYPEIVNPNdGTPLADGEQGELL---FTTL---------TKEAlpvIRY- 302
Cdd:PRK07656 318 EASGvttfnrLDDDRKTVAGTIGTAIA--GVENKIVNEL-GEEVPVGEVGELLvrgPNVMkgyyddpeaTAAA---IDAd 391
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 515953928 303 ---RTRDLTrllpgtartmrRMD-----RISGRSDDMLIIRGVNVFPSQLEEeiVKFEH 353
Cdd:PRK07656 392 gwlHTGDLG-----------RLDeegylYIVDRKKDMFIVGGFNVYPAEVEE--VLYEH 437
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
76-353 |
4.74e-09 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 57.96 E-value: 4.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 76 PFDTFAVPMEQVVRIHASSGTTGKPTVVGYTQNDIdnWANIVA-RSLRAAGGSAKDKI-------HVaygYGLFTGGLga 147
Cdd:cd05936 116 LGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNL--VANALQiKAWLEDLLEGDDVVlaalplfHV---FGLTVALL-- 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 148 hYGAeRLGATVIPMSGGQTEKQAQLIRDFQPDMIMVTP---SYCLNLIEELERqmggDASacSLRVGVFGAEPWTQAMRR 224
Cdd:cd05936 189 -LPL-ALGATIVLIPRFRPIGVLKEIRKHRVTIFPGVPtmyIALLNAPEFKKR----DFS--SLRLCISGGAPLPVEVAE 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 225 EIEKRLGITALDIYGLSEvMGPGVAMECLETAD-----GPTIWedHFYPEIVNPnDGTPLADGEQGELlfttltkealpV 299
Cdd:cd05936 261 RFEELTGVPIVEGYGLTE-TSPVVAVNPLDGPRkpgsiGIPLP--GTEVKIVDD-DGEELPPGEVGEL-----------W 325
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 515953928 300 IR--------YRTRDLT--RLLPGTART--MRRMD-----RISGRSDDMLIIRGVNVFPSQLEEEIvkFEH 353
Cdd:cd05936 326 VRgpqvmkgyWNRPEETaeAFVDGWLRTgdIGYMDedgyfFIVDRKKDMIIVGGFNVYPREVEEVL--YEH 394
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
48-289 |
8.24e-09 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 57.61 E-value: 8.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 48 GVHPDDFTELADLQKFPCTTkqdlRDNYPFDTFAVPMEQVVRIHASSGTTGKPTVVGYTQNDIDNWANIVARSLRAAGGS 127
Cdd:cd05911 113 DDKPDGVLSIEDLLSPTLGE----EDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFLYGNDGS 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 128 aKDKI-------HVaygYGLFTgglgAHYGAERlGATVIPMSGGQTEKQAQLIRDFQPDMIMVTPSYCLNLIE--ELERQ 198
Cdd:cd05911 189 -NDVIlgflplyHI---YGLFT----TLASLLN-GATVIIMPKFDSELFLDLIEKYKITFLYLVPPIAAALAKspLLDKY 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 199 mggDASacSLRVGVFGAEPWTQAMRREIEKRLGITAL-DIYGLSEvMGPGVAMecletadgpTIWEDHFYP--------- 268
Cdd:cd05911 260 ---DLS--SLRVILSGGAPLSKELQELLAKRFPNATIkQGYGMTE-TGGILTV---------NPDGDDKPGsvgrllpnv 324
|
250 260
....*....|....*....|...
gi 515953928 269 --EIVNPNDGTPLADGEQGELLF 289
Cdd:cd05911 325 eaKIVDDDGKDSLGPNEPGEICV 347
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
94-353 |
9.40e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 57.12 E-value: 9.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 94 SGTTGKPTVVGYTQndidnwANIVARSLRAAGG---SAKDKI-------HVaygyglftGGLGAHYGAERLGATVIpmsg 163
Cdd:PRK06187 176 SGTTGHPKGVVLSH------RNLFLHSLAVCAWlklSRDDVYlvivpmfHV--------HAWGLPYLALMAGAKQV---- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 164 gqtekqaqLIRDFQPDMIM-------VTPSYC----LNLIEELERQMGGDASacSLRVGVFGAEPWTQAMRREIEKRLGI 232
Cdd:PRK06187 238 --------IPRRFDPENLLdlieterVTFFFAvptiWQMLLKAPRAYFVDFS--SLRLVIYGGAALPPALLREFKEKFGI 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 233 TALDIYGLSEvMGPGVAMECLEtADGPTIWEDH-----FYP----EIVNPnDGTPLA--DGEQGELlfttltkealpVIR 301
Cdd:PRK06187 308 DLVQGYGMTE-TSPVVSVLPPE-DQLPGQWTKRrsagrPLPgveaRIVDD-DGDELPpdGGEVGEI-----------IVR 373
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515953928 302 --YRTRDLTRLLPGTARTMR----------RMD-----RISGRSDDMLIIRGVNVFPSQLEEEIVKFEH 353
Cdd:PRK06187 374 gpWLMQGYWNRPEATAETIDggwlhtgdvgYIDedgylYITDRIKDVIISGGENIYPRELEDALYGHPA 442
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
93-355 |
1.88e-08 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 56.60 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 93 SSGTTGKPTVVGYTQNDIdnWANIVARSLRAAGGsAKDKIHVAYGYGLFTGGLgahYGAE---RLGATVIPMSGGQTEKQ 169
Cdd:PRK13295 205 TSGTTGEPKGVMHTANTL--MANIVPYAERLGLG-ADDVILMASPMAHQTGFM---YGLMmpvMLGATAVLQDIWDPARA 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 170 AQLIRDFQPDMIMVTPSYCLNLIEELErQMGGDASacSLRVGVFGAEPWTQAMRREIEKRLGITALDIYGLSE-----VM 244
Cdd:PRK13295 279 AELIRTEGVTFTMASTPFLTDLTRAVK-ESGRPVS--SLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTEngavtLT 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 245 GPGVAMECLETADGptiwedhfYP------EIVNPnDGTPLADGEQGELLFTT-------LTKEALPVIR----YRTRDL 307
Cdd:PRK13295 356 KLDDPDERASTTDG--------CPlpgvevRVVDA-DGAPLPAGQIGRLQVRGcsnfggyLKRPQLNGTDadgwFDTGDL 426
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 515953928 308 TRLLPGTARtmrrmdRISGRSDDmLIIRGVNVFPSqLEEEIVKFEHLS 355
Cdd:PRK13295 427 ARIDADGYI------RISGRSKD-VIIRGGENIPV-VEIEALLYRHPA 466
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
84-288 |
2.44e-08 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 55.95 E-value: 2.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 84 MEQVVRIHASSGTTGKPTVVGYTQNDIdnWANiVARSLRAAGGSAKDKIHVAYGYGLFTGGLGAHYGAERLGATVIPMSG 163
Cdd:cd05935 83 LDDLALIPYTSGTTGLPKGCMHTHFSA--AAN-ALQSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMAR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 164 GQTEKQAQLIRDFQPDMIMVTPSYCLNLIEELERQmggDASACSLRVGVFGAEPWTQAMRREIEKRLGITALDIYGLSEV 243
Cdd:cd05935 160 WDRETALELIEKYKVTFWTNIPTMLVDLLATPEFK---TRDLSSLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTET 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 515953928 244 MGP-------GVAMECLETADGPTiwedhfYPEIVNPNDGTPLADGEQGELL 288
Cdd:cd05935 237 MSQthtnpplRPKLQCLGIP*FGV------DARVIDIETGRELPPNEVGEIV 282
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
93-350 |
7.22e-08 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 54.39 E-value: 7.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 93 SSGTTGKPTVVGYTQNDIDNWANIVARS-LRAAGGS---AKDKIHVAYGYGlftGGLgahYGAERLGATVIPMSGGQT-E 167
Cdd:cd05919 99 SSGTTGPPKGVMHAHRDPLLFADAMAREaLGLTPGDrvfSSAKMFFGYGLG---NSL---WFPLAVGASAVLNPGWPTaE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 168 KQAQLIRDFQPDMIMVTPSYCLNLIEElerQMGGDASACSLRVGVFGAEPWTQAMRREIEKRLGITALDIYGLSEVMG-- 245
Cdd:cd05919 173 RVLATLARFRPTVLYGVPTFYANLLDS---CAGSPDALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHif 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 246 ----PGVAMecLETADGPTIWedhFYPEIVNPnDGTPLADGEQGELLfttLTKEALPVIRYRTRDLTR--LLPGTARTMR 319
Cdd:cd05919 250 lsnrPGAWR--LGSTGRPVPG---YEIRLVDE-EGHTIPPGEEGDLL---VRGPSAAVGYWNNPEKSRatFNGGWYRTGD 320
|
250 260 270
....*....|....*....|....*....|....*...
gi 515953928 320 RMDRIS-------GRSDDMLIIRGVNVFPSQLEEEIVK 350
Cdd:cd05919 321 KFCRDAdgwythaGRADDMLKVGGQWVSPVEVESLIIQ 358
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
94-337 |
9.99e-08 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 54.07 E-value: 9.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 94 SGTTGKP--TVVGYtqndiDNWANIVARSLRAAGGSAKDKI--HVAYGyglFTGGLGAHYGAERLGATVIPMSGGQT--- 166
Cdd:cd05930 102 SGSTGKPkgVMVEH-----RGLVNLLLWMQEAYPLTPGDRVlqFTSFS---FDVSVWEIFGALLAGATLVVLPEEVRkdp 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 167 EKQAQLIRDFQPDMIMVTPSYCLNLIEELERQMggdasACSLRVGVFGAEPWTQAMRREIEKRL-GITALDIYGLSEVMG 245
Cdd:cd05930 174 EALADLLAEEGITVLHLTPSLLRLLLQELELAA-----LPSLRLVLVGGEALPPDLVRRWRELLpGARLVNLYGPTEATV 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 246 PGVAMECLETAD-------GPTIWEDHFYpeIVNPNdGTPLADGEQGELLFTT------------LTKE---ALPVIR-- 301
Cdd:cd05930 249 DATYYRVPPDDEedgrvpiGRPIPNTRVY--VLDEN-LRPVPPGVPGELYIGGaglargylnrpeLTAErfvPNPFGPge 325
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 515953928 302 --YRTRDLTRLLPGtartmrrmDRIS--GRSDDMLIIRGV 337
Cdd:cd05930 326 rmYRTGDLVRWLPD--------GNLEflGRIDDQVKIRGY 357
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
93-349 |
1.88e-07 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 53.14 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 93 SSGTTGKPTVVGYTQNDIDNWANIVARSLraaGGSAKDKIHVAYGYGLFTGGLG-AHYGAERLGATVIPMSGGQTEKQ-A 170
Cdd:cd05959 171 SSGSTGRPKGVVHLHADIYWTAELYARNV---LGIREDDVCFSAAKLFFAYGLGnSLTFPLSVGATTVLMPERPTPAAvF 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 171 QLIRDFQPDMIMVTPSYCLNLieeLERQMGGDASACSLRVGVFGAEPWTQAMRREIEKRLGITALDIYGLSEVMG----- 245
Cdd:cd05959 248 KRIRRYRPTVFFGVPTLYAAM---LAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLHiflsn 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 246 -PGvameclETADGPTIWEDHFYP-EIVNPnDGTPLADGEQGELLfttLTKEALPVIRYRTRDLTR--LLPGTARTMRRM 321
Cdd:cd05959 325 rPG------RVRYGTTGKPVPGYEvELRDE-DGGDVADGEPGELY---VRGPSSATMYWNNRDKTRdtFQGEWTRTGDKY 394
|
250 260 270
....*....|....*....|....*....|....*
gi 515953928 322 DR-------ISGRSDDMLIIRGVNVFPSQLEEEIV 349
Cdd:cd05959 395 VRdddgfytYAGRADDMLKVSGIWVSPFEVESALV 429
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
270-427 |
4.33e-07 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 52.24 E-value: 4.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 270 IVNPNDGTPLADGEQGELLF---------------TTLTKEALPVIR----YRTRDLTRLLpgtartmrrmDR---ISGR 327
Cdd:cd05931 368 IVDPETGRELPDGEVGEIWVrgpsvasgywgrpeaTAETFGALAATDeggwLRTGDLGFLH----------DGelyITGR 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 328 SDDMLIIRGVNVFPSQLEEEIvkfEHLSPHYqlevnRRG----------HLDSLSVKVELKQsslTLTHEQRCQVCHQLR 397
Cdd:cd05931 438 LKDLIIVRGRNHYPQDIEATA---EEAHPAL-----RPGcvaafsvpddGEERLVVVAEVER---GADPADLAAIAAAIR 506
|
170 180 190
....*....|....*....|....*....|....*.
gi 515953928 398 HRIKSMVGIS-TDVMIVNCGSIPR-SEGK----ACR 427
Cdd:cd05931 507 AAVAREHGVApADVVLVRPGSIPRtSSGKiqrrACR 542
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
93-349 |
5.65e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 51.52 E-value: 5.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 93 SSGTTGKPTVVGYTQNDIDNWANIVARSLRAaggSAKDKIHVA----YGYGLFTGGLGAHYGaerlGATVIPMSGGQTEK 168
Cdd:cd05934 89 TSGTTGPPKGVVITHANLTFAGYYSARRFGL---GEDDVYLTVlplfHINAQAVSVLAALSV----GATLVLLPRFSASR 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 169 QAQLIRDFQ----------PDMIMVTPsyclnlieELERQmggdaSACSLRVgVFGAEPwTQAMRREIEKRLGITALDIY 238
Cdd:cd05934 162 FWSDVRRYGatvtnylgamLSYLLAQP--------PSPDD-----RAHRLRA-AYGAPN-PPELHEEFEERFGVRLLEGY 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 239 GLSEVMGPGVAmecleTADGPTIW------EDHFYPEIVNPnDGTPLADGEQGELLFTTL---------------TKEAL 297
Cdd:cd05934 227 GMTETIVGVIG-----PRDEPRRPgsigrpAPGYEVRIVDD-DGQELPAGEPGELVIRGLrgwgffkgyynmpeaTAEAM 300
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 515953928 298 PVIRYRTRDLTRLLP-GTArtmrrmdRISGRSDDMLIIRGVNVFPSQLEEEIV 349
Cdd:cd05934 301 RNGWFHTGDLGYRDAdGFF-------YFVDRKKDMIRRRGENISSAEVERAIL 346
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
163-427 |
7.82e-07 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 51.16 E-value: 7.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 163 GGQTEKQAQLIRDFQPDMIMVTPSYCLNLIEELERqmgGDASACSLRVGVFGAEPWTQAMRREIEKRlGITALDIYGLSE 242
Cdd:PRK05857 246 GENTTSLLEILTTNAVATTCLVPTLLSKLVSELKS---ANATVPSLRLVGYGGSRAIAADVRFIEAT-GVRTAQVYGLSE 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 243 VmgpGVAMECLETADGPTIWEDHF-----YPEI----VNPNDGTPLADGEQGELLFTTL-TKEALPVIRY-----RTRDL 307
Cdd:PRK05857 322 T---GCTALCLPTDDGSIVKIEAGavgrpYPGVdvylAATDGIGPTAPGAGPSASFGTLwIKSPANMLGYwnnpeRTAEV 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 308 trLLPGTART----MRRMD---RISGRSDDMLIIRGVNVFPSQLEE---------EIVKFEHLSPHYqlevnrrGHLDSL 371
Cdd:PRK05857 399 --LIDGWVNTgdllERREDgffYIKGRSSEMIICGGVNIAPDEVDRiaegvsgvrEAACYEIPDEEF-------GALVGL 469
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 515953928 372 SV--KVELKQSSltlTHEQRCQVCHQLRHRIKSMVGISTDVMIVNcgsIPRSE-GKACR 427
Cdd:PRK05857 470 AVvaSAELDESA---ARALKHTIAARFRRESEPMARPSTIVIVTD---IPRTQsGKVMR 522
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
94-348 |
5.22e-06 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 48.44 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 94 SGTTGKPTVVGYTQNDIDNwaniVARSLRAAGGSAKDK--IHVA---YGYGLFTGGLGAHYgaerLGATVIPMSGGQTEK 168
Cdd:cd05941 98 SGTTGRPKGVVLTHANLAA----NVRALVDAWRWTEDDvlLHVLplhHVHGLVNALLCPLF----AGASVEFLPKFDPKE 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 169 QAQLIRDFQPDMIMVTPSYCLNLIEELER---QMGGDASAC--SLRVGVFGAEPWTQAMRREIEKRLGITALDIYGLSEV 243
Cdd:cd05941 170 VAISRLMPSITVFMGVPTIYTRLLQYYEAhftDPQFARAAAaeRLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEI 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 244 mgpGVAMECleTADGPTIwedhfyP------------EIVNPNDGTPLADGEQGEL------LFT------TLTKEALPV 299
Cdd:cd05941 250 ---GMALSN--PLDGERR------PgtvgmplpgvqaRIVDEETGEPLPRGEVGEIqvrgpsVFKeywnkpEATKEEFTD 318
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 515953928 300 IRY-RTRDLTRllpgtartmRRMD---RISGRSDDMLI-IRGVNVFPSQLEEEI 348
Cdd:cd05941 319 DGWfKTGDLGV---------VDEDgyyWILGRSSVDIIkSGGYKVSALEIERVL 363
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
70-345 |
5.61e-06 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 48.66 E-value: 5.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 70 DLRDNYPF-DTFAVPM---EQVVRIHASSGTTGKPTVVGYTQNDIDNWANIVARSLRAAGGSAKDKI------HVAYGYG 139
Cdd:cd05923 131 GLGEPESAgPLIEDPPrepEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRHNVVLglmplyHVIGFFA 210
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 140 LFTGGLGahygaerLGATVIPMSGGQTEKQAQLIRDFQPDMIMVTPSYCLNLIEELErQMGGDASacSLRVGVFGAEPWT 219
Cdd:cd05923 211 VLVAALA-------LDGTYVVVEEFDPADALKLIEQERVTSLFATPTHLDALAAAAE-FAGLKLS--SLRHVTFAGATMP 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 220 QAMRREIEKRLGITALDIYGLSEVMGPGVAmeclETADGPTIWEDHFYPEI-VNPNDGTP---LADGEQGELLFTTLTKE 295
Cdd:cd05923 281 DAVLERVNQHLPGEKVNIYGTTEAMNSLYM----RDARTGTEMRPGFFSEVrIVRIGGSPdeaLANGEEGELIVAAAADA 356
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 296 ALpvIRYRTR---DLTRLLPGTARTMRR--MD-----RISGRSDDMLIIRGVNVFPSQLE 345
Cdd:cd05923 357 AF--TGYLNQpeaTAKKLQDGWYRTGDVgyVDpsgdvRILGRVDDMIISGGENIHPSEIE 414
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
78-287 |
7.64e-06 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 48.00 E-value: 7.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 78 DTFAVPMEQ--VVRIHASSGTTGKPTVVGYT-QNDIDNWANIVArslRAAGGSAKDKI--------HVaYGYGLFTgglg 146
Cdd:cd05904 149 EPPVVVIKQddVAALLYSSGTTGRSKGVMLThRNLIAMVAQFVA---GEGSNSDSEDVflcvlpmfHI-YGLSSFA---- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 147 ahYGAERLGATVIPMSGGQTEKQAQLIRDFQPDMIMVTPSYCLNLIeelERQMGGDASACSLRVGVFGAEPWTQAMRREI 226
Cdd:cd05904 221 --LGLLRLGATVVVMPRFDLEELLAAIERYKVTHLPVVPPIVLALV---KSPIVDKYDLSSLRQIMSGAAPLGKELIEAF 295
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 515953928 227 EKRLGitALDI---YGLSEvMGPGVAMECLETADGPTI---------WEdhfyPEIVNPNDGTPLADGEQGEL 287
Cdd:cd05904 296 RAKFP--NVDLgqgYGMTE-STGVVAMCFAPEKDRAKYgsvgrlvpnVE----AKIVDPETGESLPPNQTGEL 361
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
93-352 |
4.68e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 45.50 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 93 SSGTTGKPTVVGYTQNDIDNWANIVARSLRAAGGS---AKDKIHVAYGyglFTGGLGAHYGaerlGATVIPMSGGQTEKQ 169
Cdd:PRK06164 189 TSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAvllAALPFCGVFG---FSTLLGALAG----GAPLVCEPVFDAART 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 170 AQLIRDFQpdmimVTPSYCLN-LIEELERQMGGDASACSLRVgvFGAEPWTQAMRR---EIEKRlGITALDIYGLSEVMg 245
Cdd:PRK06164 262 ARALRRHR-----VTHTFGNDeMLRRILDTAGERADFPSARL--FGFASFAPALGElaaLARAR-GVPLTGLYGSSEVQ- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 246 pgvAMECLETADGPtiWEDHF-------YPE----IVNPNDGTPLADGEQGEL------LFTTL------TKEALPVIRY 302
Cdd:PRK06164 333 ---ALVALQPATDP--VSVRIegggrpaSPEarvrARDPQDGALLPDGESGEIeirapsLMRGYldnpdaTARALTDDGY 407
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 515953928 303 -RTRDLTRLLPGTARTMRrmdrisGRSDDMLIIRGVNVFPSQLEEEIVKFE 352
Cdd:PRK06164 408 fRTGDLGYTRGDGQFVYQ------TRMGDSLRLGGFLVNPAEIEHALEALP 452
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
94-286 |
8.83e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 44.57 E-value: 8.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 94 SGTTGKPTVVGYTQNDIdnWANIVARSLraAGGSAKDKIHVAYgYGLF--TGGLGAHYGAERLGATVIPMSGGQTEKQAQ 171
Cdd:PRK08314 199 SGTTGVPKGCMHTHRTV--MANAVGSVL--WSNSTPESVVLAV-LPLFhvTGMVHSMNAPIYAGATVVLMPRWDREAAAR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 172 LIRDFQ-------PDMI---MVTP---SYCLNlieelerqmggdasacSLRVGVFGAEPWTQAMRREIEKRLGITALDIY 238
Cdd:PRK08314 274 LIERYRvthwtniPTMVvdfLASPglaERDLS----------------SLRYIGGGGAAMPEAVAERLKELTGLDYVEGY 337
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 515953928 239 GLSEVMGPGVA-------MECLetadG-PTIWEDhfyPEIVNPNDGTPLADGEQGE 286
Cdd:PRK08314 338 GLTETMAQTHSnppdrpkLQCL----GiPTFGVD---ARVIDPETLEELPPGEVGE 386
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
93-348 |
2.67e-04 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 43.20 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 93 SSGTTGKPTVVGYTQNDIDNWANIVARSLraaGGSAKDKIHVA----YGYGLFTggLGAHYgaERLGATVIPMSGGQTEK 168
Cdd:cd05922 125 TSGSTGSPKLVRLSHQNLLANARSIAEYL---GITADDRALTVlplsYDYGLSV--LNTHL--LRGATLVLTNDGVLDDA 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 169 QAQLIRDFQPDMIMVTPSyclnLIEELERQMGGDASACSLRVgvfgaepWTQA---MRREIEKRL-----GITALDIYGL 240
Cdd:cd05922 198 FWEDLREHGATGLAGVPS----TYAMLTRLGFDPAKLPSLRY-------LTQAggrLPQETIARLrellpGAQVYVMYGQ 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 241 SE------VMGPGVAMECLETAdGPTIWEDHFypEIVNPnDGTPLADGEQGELLFT-------------TLTKEALPVIR 301
Cdd:cd05922 267 TEatrrmtYLPPERILEKPGSI-GLAIPGGEF--EILDD-DGTPTPPGEPGEIVHRgpnvmkgywndppYRRKEGRGGGV 342
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 515953928 302 YRTRDLTRllpgtartmRRMD---RISGRSDDMLIIRGVNVFPSQLEEEI 348
Cdd:cd05922 343 LHTGDLAR---------RDEDgflFIVGRRDRMIKLFGNRISPTEIEAAA 383
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
324-350 |
7.46e-04 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 41.24 E-value: 7.46e-04
10 20
....*....|....*....|....*..
gi 515953928 324 ISGRSDDMLIIRGVNVFPSQLEEEIVK 350
Cdd:cd17633 226 LVGRESDMIIIGGINIFPTEIESVLKA 252
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
94-346 |
1.58e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 40.75 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 94 SGTTGKPTVVGYTQndidnwANIVARSL--RAAGGSAKDKIHVAYG-------YGLftgglgahygaeRLGATVIPMSGG 164
Cdd:PRK05605 228 SGTTGKPKGAQLTH------RNLFANAAqgKAWVPGLGDGPERVLAalpmfhaYGL------------TLCLTLAVSIGG 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 165 QTekqaQLIRDFQPDMIM-------------VTPSYcLNLIEELERQmggDASACSLRVGVFGAEPWTQAMRREIEKRLG 231
Cdd:PRK05605 290 EL----VLLPAPDIDLILdamkkhpptwlpgVPPLY-EKIAEAAEER---GVDLSGVRNAFSGAMALPVSTVELWEKLTG 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 232 ITALDIYGLSEV--------MGP-------GVAMECLETadgptiwedhfypEIVNPND-GTPLADGEQGELLfttltke 295
Cdd:PRK05605 362 GLLVEGYGLTETspiivgnpMSDdrrpgyvGVPFPDTEV-------------RIVDPEDpDETMPDGEEGELL------- 421
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 515953928 296 alpvIR-------YRTR-DLTR--LLPGTART--MRRMD-----RISGRSDDMLIIRGVNVFPSQLEE 346
Cdd:PRK05605 422 ----VRgpqvfkgYWNRpEETAksFLDGWFRTgdVVVMEedgfiRIVDRIKELIITGGFNVYPAEVEE 485
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
207-288 |
4.15e-03 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 39.52 E-value: 4.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515953928 207 SLRVGVFGAEPWTQAMRREIEKRLGITALDIYGLSEvMGPGVAMECLETADgPTIWEDHFYPE-------------IVNP 273
Cdd:PRK08633 899 SLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGATE-TSPVASVNLPDVLA-ADFKRQTGSKEgsvgmplpgvavrIVDP 976
|
90
....*....|....*
gi 515953928 274 NDGTPLADGEQGELL 288
Cdd:PRK08633 977 ETFEELPPGEDGLIL 991
|
|
| |
